SitesBLAST
Comparing Ga0059261_0771 FitnessBrowser__Korea:Ga0059261_0771 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
Q4WR83 Acyl-CoA ligase sidI; Siderophore biosynthesis protein I; EC 6.2.1.- from Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata) (see paper)
41% identity, 99% coverage: 8:553/554 of query aligns to 23:590/590 of Q4WR83
Sites not aligning to the query:
- 6:14 PTS2-type peroxisomal targeting signal
P69451 Long-chain-fatty-acid--CoA ligase; Long-chain acyl-CoA synthetase; Acyl-CoA synthetase; EC 6.2.1.3 from Escherichia coli (strain K12) (see paper)
33% identity, 94% coverage: 15:533/554 of query aligns to 12:551/561 of P69451
- Y213 (≠ F193) mutation to A: Loss of activity.
- T214 (= T194) mutation to A: 10% of wild-type activity.
- G216 (= G196) mutation to A: Decreases activity.
- T217 (= T197) mutation to A: Decreases activity.
- G219 (= G199) mutation to A: Decreases activity.
- K222 (= K202) mutation to A: Decreases activity.
- E361 (= E339) mutation to A: Loss of activity.
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
33% identity, 89% coverage: 42:533/554 of query aligns to 21:499/506 of 4gxqA
- active site: T163 (= T194), N183 (= N214), H207 (= H238), T303 (= T338), E304 (= E339), I403 (= I440), N408 (= N445), A491 (≠ K525)
- binding adenosine-5'-triphosphate: T163 (= T194), S164 (= S195), G165 (= G196), T166 (= T197), T167 (= T198), H207 (= H238), S277 (≠ P315), A278 (≠ E316), P279 (= P317), E298 (≠ I333), M302 (= M337), T303 (= T338), D382 (= D419), R397 (= R434)
- binding carbonate ion: H207 (= H238), S277 (≠ P315), R299 (≠ G334), G301 (= G336)
6k4cA Ancestral luciferase anclamp in complex with dlsa (see paper)
29% identity, 94% coverage: 18:535/554 of query aligns to 14:537/538 of 6k4cA
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: H243 (= H238), F245 (= F240), T249 (≠ G245), G314 (= G311), A315 (= A312), P316 (≠ I313), G337 (= G334), Y338 (= Y335), G339 (= G336), L340 (≠ M337), T341 (= T338), A346 (≠ V343), D420 (= D419), I432 (= I431), K527 (= K525)
6k4dA Ancestral luciferase anclamp in complex with atp and d-luciferin (see paper)
29% identity, 94% coverage: 18:535/554 of query aligns to 14:537/539 of 6k4dA
- binding [[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl] (4S)-2-(6-oxidanyl-1,3-benzothiazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylate: H243 (= H238), F245 (= F240), T249 (≠ G245), G314 (= G311), A315 (= A312), P316 (≠ I313), G337 (= G334), Y338 (= Y335), G339 (= G336), L340 (≠ M337), T341 (= T338), S345 (≠ P342), A346 (≠ V343), D420 (= D419), I432 (= I431), K527 (= K525)
- binding (4S)-2-(6-hydroxy-1,3-benzothiazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid: F245 (= F240), R335 (≠ T332), G337 (= G334), G339 (= G336), L340 (≠ M337), A346 (≠ V343)
Q9S725 4-coumarate--CoA ligase 2; 4CL 2; 4-coumarate--CoA ligase isoform 2; At4CL2; 4-coumaroyl-CoA synthase 2; Caffeate--CoA ligase; EC 6.2.1.12; EC 6.2.1.- from Arabidopsis thaliana (Mouse-ear cress) (see 3 papers)
29% identity, 90% coverage: 34:532/554 of query aligns to 48:547/556 of Q9S725
- K211 (= K202) mutation to S: Drastically reduces the activity.
- M293 (≠ Y281) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ M309) mutation K->L,A: Affects the substrate specificity.
- E401 (= E386) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (= C388) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R434) mutation to Q: Drastically reduces the activity.
- K457 (≠ G442) mutation to S: Drastically reduces the activity.
- K540 (= K525) mutation to N: Abolishes the activity.
2d1sA Crystal structure of the thermostable japanese firefly luciferase complexed with high-energy intermediate analogue (see paper)
30% identity, 94% coverage: 18:535/554 of query aligns to 13:535/539 of 2d1sA
- active site: S194 (≠ T194), R214 (≠ N214), H241 (= H238), T339 (= T338), E340 (= E339), K439 (≠ I440), Q444 (≠ N445), K525 (= K525)
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: S194 (≠ T194), S195 (= S195), H241 (= H238), F243 (= F240), T247 (≠ G245), I282 (≠ Y281), G312 (= G311), A313 (= A312), P314 (≠ I313), Q334 (≠ I333), G335 (= G334), Y336 (= Y335), G337 (= G336), L338 (≠ M337), T339 (= T338), S343 (≠ P342), A344 (≠ V343), D418 (= D419), R433 (= R434), K525 (= K525)
2d1rA Crystal structure of the thermostable japanese firefly luciferase complexed with oxyluciferin and amp (see paper)
30% identity, 94% coverage: 18:535/554 of query aligns to 13:535/539 of 2d1rA
- active site: S194 (≠ T194), R214 (≠ N214), H241 (= H238), T339 (= T338), E340 (= E339), K439 (≠ I440), Q444 (≠ N445), K525 (= K525)
- binding adenosine monophosphate: S194 (≠ T194), S195 (= S195), H241 (= H238), G312 (= G311), A313 (= A312), P314 (≠ I313), G335 (= G334), Y336 (= Y335), G337 (= G336), L338 (≠ M337), T339 (= T338), D418 (= D419), K525 (= K525)
- binding 2-(6-hydroxy-1,3-benzothiazol-2-yl)-1,3-thiazol-4(5h)-one: H241 (= H238), F243 (= F240), T247 (≠ G245), G335 (= G334), G337 (= G336), L338 (≠ M337), A344 (≠ V343)
Q84P21 Peroxisomal OPC-8:0-CoA ligase 1; 4-coumarate--CoA ligase isoform 9; At4CL9; 4-coumarate--CoA ligase-like 5; EC 6.2.1.- from Arabidopsis thaliana (Mouse-ear cress) (see paper)
28% identity, 90% coverage: 38:534/554 of query aligns to 46:540/546 of Q84P21
- K530 (= K525) mutation to N: Lossed enzymatic activity.
O24146 4-coumarate--CoA ligase 2; 4CL 2; Nt4CL-19; Nt4CL-2; 4-coumaroyl-CoA synthase 2; Caffeate--CoA ligase; Cinnamate--CoA ligase; Ferulate--CoA ligase; EC 6.2.1.12; EC 6.2.1.-; EC 6.2.1.-; EC 6.2.1.34 from Nicotiana tabacum (Common tobacco) (see paper)
29% identity, 91% coverage: 34:539/554 of query aligns to 37:540/542 of O24146
- S189 (≠ T194) binding
- S190 (= S195) binding
- G191 (= G196) binding
- T192 (= T197) binding
- T193 (= T198) binding ; mutation to A: Reduced activity against 4-coumarate.
- K197 (= K202) binding ; mutation to A: Reduced activity against 4-coumarate.
- H237 (= H238) mutation to A: Strongly reduced activity against 4-coumarate.
- Y239 (≠ F240) binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.; mutation to F: Reduced activity against 4-coumarate.
- S243 (≠ M244) binding ; binding ; binding
- K260 (≠ G262) binding
- A309 (= A312) binding ; binding ; binding
- Q331 (≠ I333) binding
- G332 (= G334) binding ; binding ; binding ; binding ; binding
- T336 (= T338) binding ; binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- V341 (= V343) mutation to G: Reduced activity against 4-coumarate.; mutation Missing: Reduced activity against 4-coumarate, but acquired ability to use sinapate as substrate.
- M344 (≠ F345) binding ; binding ; binding ; mutation to A: Reduced activity against 4-coumarate.
- D420 (= D419) binding ; binding ; binding ; binding ; binding
- R435 (= R434) binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- K437 (= K436) binding ; binding ; binding ; binding
- K441 (≠ I440) binding ; binding ; binding ; binding ; mutation to A: Abolished activity against 4-coumarate.
- K443 (≠ G442) binding ; mutation to A: Normal activity against 4-coumarate.
- G444 (= G443) binding
- Q446 (≠ N445) binding
- K526 (= K525) binding ; mutation to A: Abolished activity against 4-coumarate.
5bsrA Crystal structure of 4-coumarate:coa ligase complexed with adenosine monophosphate and coenzyme a (see paper)
29% identity, 91% coverage: 34:535/554 of query aligns to 29:528/528 of 5bsrA
- active site: S181 (≠ T194), S201 (≠ N214), H229 (= H238), T328 (= T338), E329 (= E339), K433 (≠ I440), Q438 (≠ N445), K518 (= K525)
- binding adenosine monophosphate: A301 (= A312), G326 (= G336), T328 (= T338), D412 (= D419), K429 (= K436), K433 (≠ I440), Q438 (≠ N445)
- binding coenzyme a: L102 (≠ A107), P226 (= P235), H229 (= H238), Y231 (≠ F240), F253 (= F263), K435 (≠ G442), G436 (= G443), F437 (≠ E444), F498 (≠ H505)
5bsvA Crystal structure of 4-coumarate:coa ligase complexed with feruloyl adenylate (see paper)
29% identity, 91% coverage: 34:535/554 of query aligns to 30:529/529 of 5bsvA
- active site: S182 (≠ T194), S202 (≠ N214), H230 (= H238), T329 (= T338), E330 (= E339), K434 (≠ I440), Q439 (≠ N445), K519 (= K525)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(5-methoxy-4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H238), Y232 (≠ F240), S236 (≠ M244), A302 (= A312), A303 (≠ E316), P304 (= P317), G325 (= G334), G327 (= G336), M328 (= M337), T329 (= T338), P333 (= P342), V334 (= V343), D413 (= D419), K430 (= K436), K434 (≠ I440), Q439 (≠ N445)
5bsuA Crystal structure of 4-coumarate:coa ligase complexed with caffeoyl adenylate (see paper)
29% identity, 91% coverage: 34:535/554 of query aligns to 30:529/529 of 5bsuA
- active site: S182 (≠ T194), S202 (≠ N214), H230 (= H238), T329 (= T338), E330 (= E339), K434 (≠ I440), Q439 (≠ N445), K519 (= K525)
- binding 5'-O-[(R)-{[(2E)-3-(3,4-dioxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}(hydroxy)phosphoryl]adenosine: H230 (= H238), Y232 (≠ F240), S236 (≠ M244), M299 (= M309), A302 (= A312), A303 (≠ E316), P304 (= P317), G325 (= G334), G327 (= G336), M328 (= M337), T329 (= T338), P333 (= P342), D413 (= D419), K430 (= K436), K434 (≠ I440), Q439 (≠ N445)
5bstA Crystal structure of 4-coumarate:coa ligase complexed with coumaroyl adenylate (see paper)
29% identity, 91% coverage: 34:535/554 of query aligns to 30:529/529 of 5bstA
- active site: S182 (≠ T194), S202 (≠ N214), H230 (= H238), T329 (= T338), E330 (= E339), K434 (≠ I440), Q439 (≠ N445), K519 (= K525)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H238), Y232 (≠ F240), S236 (≠ M244), A302 (= A312), A303 (≠ E316), P304 (= P317), G325 (= G334), Y326 (= Y335), G327 (= G336), M328 (= M337), T329 (= T338), P333 (= P342), V334 (= V343), D413 (= D419), K430 (= K436), K434 (≠ I440), Q439 (≠ N445)
5bsmA Crystal structure of 4-coumarate:coa ligase complexed with magnesium and adenosine triphosphate (see paper)
29% identity, 91% coverage: 34:535/554 of query aligns to 30:529/530 of 5bsmA
- active site: S182 (≠ T194), S202 (≠ N214), H230 (= H238), T329 (= T338), E330 (= E339), K434 (≠ I440), Q439 (≠ N445), K519 (= K525)
- binding adenosine-5'-triphosphate: S182 (≠ T194), S183 (= S195), G184 (= G196), T185 (= T197), T186 (= T198), K190 (= K202), H230 (= H238), A302 (= A312), A303 (≠ E316), P304 (= P317), Y326 (= Y335), G327 (= G336), M328 (= M337), T329 (= T338), D413 (= D419), I425 (= I431), R428 (= R434), K519 (= K525)
P9WQ37 Long-chain-fatty-acid--CoA ligase FadD13; Fatty acyl-CoA ligase; FACL; FACL13; Fatty acyl-CoA synthetase; ACS; FACS; Very-long-chain fatty-acyl-CoA synthetase; ACSVL; EC 6.2.1.3 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 4 papers)
28% identity, 89% coverage: 40:533/554 of query aligns to 20:495/503 of P9WQ37
- K172 (= K202) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ S225) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ Q227) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ C239) mutation to D: Strong reduction of the fatty acyl-CoA ligase activity. No significant change in the total expression level, however the cytoplasmic expression is reduced. Slight increase of susceptibility to proteolysis.
- A211 (≠ G241) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ M244) mutation to W: Shows a marked decrease in the activity with lauric and palmitic acid (C12 and C16 fatty acid) with a simultaneous increase in the activity with caprylic acid (C8 fatty acid).
- R244 (= R276) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G336) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.; mutation to W: Does not show activity with small, medium or long acyl chains.
- W377 (= W414) mutation to A: Strong reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding. No significant change in the total expression level, however the cytoplasmic expression is low. Slight increase of susceptibility to proteolysis.
- D382 (= D419) mutation to A: Strong reduction of the fatty acyl-CoA ligase activity. No significant change in the total expression level, however the cytoplasmic expression is reduced.
- R397 (= R434) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (≠ R441) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G443) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K525) mutation to A: Strong reduction of the fatty acyl-CoA ligase activity. Reduction of binding affinity for ATP.
Sites not aligning to the query:
- 9 R→A: Alteration of the strength of the membrane binding; when associated with A-9; A-195; A-197 and A-244.
- 17 R→A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
3ni2A Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate:coa ligase (see paper)
29% identity, 90% coverage: 38:533/554 of query aligns to 34:527/528 of 3ni2A
- active site: S182 (≠ T194), S202 (vs. gap), H230 (= H238), T329 (= T338), E330 (= E339), K434 (≠ I440), Q439 (≠ N445), K519 (= K525)
- binding 5'-O-{(S)-hydroxy[3-(4-hydroxyphenyl)propoxy]phosphoryl}adenosine: Y232 (≠ F240), S236 (≠ M244), G302 (= G311), A303 (= A312), P304 (= P317), G325 (= G334), G327 (= G336), T329 (= T338), P333 (= P342), V334 (= V343), D413 (= D419), K430 (= K436), K434 (≠ I440), Q439 (≠ N445)
3a9vA Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate--coa ligase (see paper)
29% identity, 90% coverage: 38:533/554 of query aligns to 34:527/528 of 3a9vA
- active site: S182 (≠ T194), S202 (vs. gap), H230 (= H238), T329 (= T338), E330 (= E339), K434 (≠ I440), Q439 (≠ N445), K519 (= K525)
- binding adenosine monophosphate: H230 (= H238), G302 (= G311), A303 (= A312), P304 (= P317), Y326 (= Y335), G327 (= G336), M328 (= M337), T329 (= T338), D413 (= D419), K430 (= K436), K434 (≠ I440), Q439 (≠ N445)
6hpsA Near-infrared dual bioluminescence imaging in vivo using infra- luciferin (see paper)
28% identity, 94% coverage: 18:536/554 of query aligns to 12:536/539 of 6hpsA
- active site: S194 (≠ T194), R214 (vs. gap), H241 (= H238), T339 (= T338), E340 (= E339), K439 (≠ I440), Q444 (≠ N445), K525 (= K525)
- binding [(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl ~{N}-[[2-[(~{E})-2-(6-oxidanyl-1,3-benzothiazol-2-yl)ethenyl]-1,3-thiazol-4-yl]carbonyl]sulfamate: H241 (= H238), G242 (≠ C239), F243 (= F240), S310 (≠ M309), G312 (= G311), A313 (= A312), P314 (≠ I313), R333 (≠ T332), G335 (= G334), Y336 (= Y335), G337 (= G336), L338 (≠ M337), T339 (= T338), A344 (≠ V343), D418 (= D419), K525 (= K525)
6q2mA Crystal structure of photinus pyralis luciferase pps6 mutant in complex with dlsa (see paper)
28% identity, 94% coverage: 18:536/554 of query aligns to 15:539/544 of 6q2mA
- active site: S197 (≠ T194), R217 (vs. gap), H244 (= H238), T342 (= T338), E343 (= E339), K442 (≠ I440), Q447 (≠ N445), K528 (= K525)
- binding (2S,5S)-hexane-2,5-diol: D18 (≠ E21), G19 (≠ H22), D186 (vs. gap), R187 (vs. gap), R260 (≠ A255), Y279 (≠ E275)
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: S198 (= S195), H244 (= H238), F246 (= F240), T250 (≠ G245), G315 (= G311), A316 (= A312), P317 (≠ I313), G338 (= G334), Y339 (= Y335), G340 (= G336), L341 (≠ M337), T342 (= T338), S346 (≠ P342), A347 (≠ V343), D421 (= D419), K528 (= K525)
Query Sequence
>Ga0059261_0771 FitnessBrowser__Korea:Ga0059261_0771
MSFVTPGLSHVRGTDTPPLIEHTIGEALVRAAEQWGERDALVSVAQGIRWSFAELLARTD
RLASGLLALGLKPGERIGIWSPNCAEWTLTQFAAARAGLILVTINPAYRLSEVEYTINKV
GLAALVAAESFKTSAYAEMVETLGPERLPTLRARILIGENERPGWLSFADVAAHLAGALP
EDLHPSDPINIQFTSGTTGLPKGATLSHRNILNNGYFVGRGMGLSAQDRICIPVPLYHCF
GMVMGNLASLTHGAAMVYPAPGFDPEAALRAVAAERCTALYGVPTMFIAMLAHPVLDSLD
VTSLRTGCMAGAICPEPLMREVIDRLHMRDVTIGYGMTETSPVSFQTALDDPIHRRTGSI
GRVQPHLESKLIDLDGNIVPVGQPGELCTRGYSVMHGYWDEQERTAESIDAEGWMHSGDL
AVIDDEGYANIVGRLKDMVIRGGENIYPREIEGFLYSHPAIEDVAVVGVPDDRMGEELCA
WVRLRAGAQADAESIRDFCRGQIAHFKVPRYVRIVAEFPTTVTGKVQKFLIREAMIAELG
SQSGAQSAETKENQ
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SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory